Malonyl-CoA O-methyltransferase

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Malonyl-CoA O-methyltransferase
Identifiers
EC no. 2.1.1.197
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Malonyl-CoA O-methyltransferase (EC 2.1.1.197, BioC) is an enzyme with systematic name S-adenosyl-L-methionine:malonyl-CoA O-methyltransferase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + malonyl-CoA S-adenosyl-L-homocysteine + malonyl-CoA methyl ester

Malonyl-CoA O-methyltransferase is involved in an early step of biotin biosynthesis in Gram-negative bacteria.

Related Research Articles

<span class="mw-page-title-main">DNA adenine methylase</span> Prokaryotic enzyme

DNA adenine methylase, (Dam methylase) (also site-specific DNA-methyltransferase (adenine-specific), EC 2.1.1.72, modification methylase, restriction-modification system) is an enzyme that adds a methyl group to the adenine of the sequence 5'-GATC-3' in newly synthesized DNA. Immediately after DNA synthesis, the daughter strand remains unmethylated for a short time. It is an orphan methyltransferase that is not part of a restriction-modification system and regulates gene expression. This enzyme catalyses the following chemical reaction

In enzymology, a tRNA guanosine-2'-O-methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Biotin synthase</span> Enzyme

Biotin synthase (BioB) is an enzyme that catalyzes the conversion of dethiobiotin (DTB) to biotin; this is the final step in the biotin biosynthetic pathway. Biotin, also known as vitamin B7, is a cofactor used in carboxylation, decarboxylation, and transcarboxylation reactions in many organisms including humans. Biotin synthase is an S-Adenosylmethionine (SAM) dependent enzyme that employs a radical mechanism to thiolate dethiobiotin, thus converting it to biotin.

<span class="mw-page-title-main">Cobalamin biosynthesis</span>

Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.

Radical SAM is a designation for a superfamily of enzymes that use a [4Fe-4S]+ cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical (5'-dAdo), as a critical intermediate. These enzymes utilize this radical intermediate to perform diverse transformations, often to functionalize unactivated C-H bonds. Radical SAM enzymes are involved in cofactor biosynthesis, enzyme activation, peptide modification, post-transcriptional and post-translational modifications, metalloprotein cluster formation, tRNA modification, lipid metabolism, biosynthesis of antibiotics and natural products etc. The vast majority of known radical SAM enzymes belong to the radical SAM superfamily, and have a cysteine-rich motif that matches or resembles CxxxCxxC. rSAMs comprise the largest superfamily of metal-containing enzymes.

<span class="mw-page-title-main">Uroporphyrinogen-III C-methyltransferase</span> Class of enzymes

Uroporphyrinogen-III C-methyltransferase, uroporphyrinogen methyltransferase, uroporphyrinogen-III methyltransferase, adenosylmethionine-uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase, uroporphyrinogen-III methylase, SirA, CysG, CobA, uroporphyrin-III C-methyltransferase, S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase. This enzyme catalyses the following chemical reaction

Demethylmenaquinone methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:demethylmenaquinone methyltransferase. This enzyme catalyses the following chemical reaction

Methyl halide transferase is an enzyme with systematic name S-adenosylmethionine:iodide methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uridine2552-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (guanine1207-N2)-methyltransferase (EC 2.1.1.172, m2G1207 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine1207-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (adenine1408-N1)-methyltransferase (EC 2.1.1.180, kanamycin-apramycin resistance methylase, 16S rRNA:m1A1408 methyltransferase, KamB, NpmA, 16S rRNA m1A1408 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1408-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase (EC 2.1.1.182, S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase, KsgA, ksgA methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanosine2251-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanosine2251-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine745-N1)-methyltransferase (EC 2.1.1.187, Rlma(I), Rlma1, 23S rRNA m1G745 methyltransferase, YebH, RlmAI methyltransferase, ribosomal RNA(m1G)-methylase, rRNA(m1G)methylase, RrmA, 23S rRNA:m1G745 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine745-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uracil1939-C5)-methyltransferase (EC 2.1.1.190, RumA, RNA uridine methyltransferase A, YgcA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil1939-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (cytidine32/uridine32-2'-O)-methyltransferase (EC 2.1.1.200, YfhQ, tRNA:Cm32/Um32 methyltransferase, TrMet(Xm32), TrmJ) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytidine32/uridine32-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

tRNA (cytidine34-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytidine34/5-carboxymethylaminomethyluridine34-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

tRNA (guanine37-N1)-methyltransferase (EC 2.1.1.228, TrmD, tRNA (m1G37) methyltransferase, transfer RNA (m1G37) methyltransferase, Trm5p, TRMT5, tRNA-(N1G37) methyltransferase, MJ0883 (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine37-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

Erythromycin 3''-O-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:erythromycin C 3''-O-methyltransferase. This enzyme catalyses the following chemical reaction

Tellurite methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:tellurite methyltransferase. This enzyme catalyses the following chemical reaction

References

  1. Del Campillo-Campbell A, Kayajanian G, Campbell A, Adhya S (December 1967). "Biotin-requiring mutants of Escherichia coli K-12". Journal of Bacteriology. 94 (6): 2065–6. PMC   276941 . PMID   4864413.
  2. Rolfe B, Eisenberg MA (August 1968). "Genetic and biochemical analysis of the biotin loci of Escherichia coli K-12". Journal of Bacteriology. 96 (2): 515–24. PMC   252325 . PMID   4877129.
  3. Otsuka AJ, Buoncristiani MR, Howard PK, Flamm J, Johnson C, Yamamoto R, Uchida K, Cook C, Ruppert J, Matsuzaki J (December 1988). "The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon". The Journal of Biological Chemistry. 263 (36): 19577–85. PMID   3058702.
  4. Cleary PP, Campbell A (November 1972). "Deletion and complementation analysis of biotin gene cluster of Escherichia coli". Journal of Bacteriology. 112 (2): 830–9. PMC   251493 . PMID   4563978.
  5. Lin S, Hanson RE, Cronan JE (September 2010). "Biotin synthesis begins by hijacking the fatty acid synthetic pathway". Nature Chemical Biology. 6 (9): 682–8. doi:10.1038/nchembio.420. PMC   2925990 . PMID   20693992.